Splanchnic utilization of enteral alanine in humans

被引:17
作者
Battezzati, A
Haisch, M
Brillon, DJ
Matthews, DE
机构
[1] Univ Vermont, Dept Med, Burlington, VT 05405 USA
[2] Cornell Univ, Coll Med, Dept Med, New York, NY USA
[3] Ist Sci San Raffaele, Milan, Italy
来源
METABOLISM-CLINICAL AND EXPERIMENTAL | 1999年 / 48卷 / 07期
关键词
D O I
10.1016/S0026-0495(99)90229-9
中图分类号
R5 [内科学];
学科分类号
1002 [临床医学]; 100201 [内科学];
摘要
The splanchnic bed extracts the majority of the enteral nonessential amino acids glutamine and glutamate, while extracting a much smaller proportion of essential amino acids such as leucine and phenylalanine. Alanine is an abundant nonessential amino acid that plays an important role in hepatic gluconeogenesis and ureagenesis. However, its enteral fate has not been studied. Twelve normal healthy postabsorptive adults received a 7-hour infusion of [1-C-13]alanine, 3.5 hours intravenously (IV) and 3.5 hours via a nasogastric tube (NG). The order of infusion was randomized among subjects. Alanine kinetics were calculated from the enrichments of plasma alanine C-13 and expired (CO2)-C-13. The alanine appearance rate (R-a), measured during the IV tracer infusion, was 279 +/- 17 mu mol/kg/h; 92% +/- 2% of the IV-infused and 86% +/- 2% of the NO-infused [1-C-13]alanine tracer was recovered as (CO2)-C-13. From the difference in plasma alanine C-13 enrichment between IV-infused and NG-infused tracers, we determined that the splanchnic bed extracted 69% +/- 1% of the enterally delivered alanine tracer on the first pass during absorption. Only one third of the enteral alanine passed intact through the splanchnic bed and was made available to systemic tissues. Of the enteral alanine extracted, 83% +/- 3% of the carboxyl-carbon label was recovered as CO2, leaving only 17% of the sequestered alanine available for use in splanchnic protein synthesis. Thus, the splanchnic bed, presumably the liver, extracts and metabolizes most of the enterally delivered alanine. Copyright (C) 1999 by W.B. Saunders Company.
引用
收藏
页码:915 / 921
页数:7
相关论文
共 34 条
[1]
TRACER PRIMING BICARBONATE POOL [J].
ALLSOP, JR ;
WOLFE, RR ;
BURKE, JF .
JOURNAL OF APPLIED PHYSIOLOGY, 1978, 45 (01) :137-139
[2]
OXIDATION OF GLUTAMIC-ACID BY THE SPLANCHNIC BED IN HUMANS [J].
BATTEZZATI, A ;
BRILLON, DJ ;
MATTHEWS, DE .
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM, 1995, 269 (02) :E269-E276
[3]
LEUCINE AND PHENYLALANINE KINETICS DURING MIXED MEAL INGESTION - A MULTIPLE TRACER APPROACH [J].
BIOLO, G ;
TESSARI, P ;
INCHIOSTRO, S ;
BRUTTOMESSO, D ;
FONGHER, C ;
SABADIN, L ;
FRATTON, MG ;
VALERIO, A ;
TIENGO, A .
AMERICAN JOURNAL OF PHYSIOLOGY, 1992, 262 (04) :E455-E463
[4]
REGULATION OF POSTPRANDIAL WHOLE-BODY PROTEOLYSIS IN INSULIN-DEPRIVED IDDM [J].
BIOLO, G ;
INCHIOSTRO, S ;
TIENGO, A ;
TESSARI, P .
DIABETES, 1995, 44 (02) :203-209
[5]
ROLE OF GLUTAMINE IN ADAPTATIONS IN NITROGEN-METABOLISM DURING FASTING [J].
CERSOSIMO, E ;
WILLIAMS, PE ;
RADOSEVICH, PM ;
HOXWORTH, BT ;
LACY, WW ;
ABUMRAD, NN .
AMERICAN JOURNAL OF PHYSIOLOGY, 1986, 250 (06) :E622-E628
[6]
GLUCONEOGENESIS FROM ALANINE IN NORMAL POSTABSORPTIVE MAN - INTRAHEPATIC STIMULATORY EFFECT OF GLUCAGON [J].
CHIASSON, JL ;
LILJENQUIST, JE ;
SINCLAIRSMITH, BC ;
LACY, WW .
DIABETES, 1975, 24 (06) :574-584
[7]
CONTRIBUTION OF LIVER AND SKELETAL-MUSCLE TO ALANINE AND LACTATE METABOLISM IN HUMANS [J].
CONSOLI, A ;
NURJHAN, N ;
REILLY, JJ ;
BIER, DM ;
GERICH, JE .
AMERICAN JOURNAL OF PHYSIOLOGY, 1990, 259 (05) :E677-E684
[8]
PLASMA AMINO-ACID KINETICS DURING ACUTE STATES OF GLUCAGON DEFICIENCY AND EXCESS IN HEALTHY-ADULTS [J].
COUET, C ;
FUKAGAWA, NK ;
MATTHEWS, DE ;
BIER, DM ;
YOUNG, VR .
AMERICAN JOURNAL OF PHYSIOLOGY, 1990, 258 (01) :E78-E85
[9]
Non-invasive tracing of liver intermediary metabolism in normal subjects and in moderately hyperglycaemic NIDDM subjects. Evidence against increased gluconeogenesis and hepatic fatty acid oxidation in NIDDM [J].
Diraison, F ;
Large, V ;
Brunengraber, H ;
Beylot, M .
DIABETOLOGIA, 1998, 41 (02) :212-220
[10]
AMINO-ACID METABOLISM IN MAN [J].
FELIG, P .
ANNUAL REVIEW OF BIOCHEMISTRY, 1975, 44 :933-955